6yba
From Proteopedia
HAdV-F41 Capsid
Structural highlights
FunctionCAPSH_ADE41 Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus.[HAMAP-Rule:MF_04051] Publication Abstract from PubMedEnteric adenoviruses, one of the main causes of viral gastroenteritis in the world, must withstand the harsh conditions found in the gut. This requirement suggests that capsid stability must be different from that of other adenoviruses. We report the 4-A-resolution structure of a human enteric adenovirus, HAdV-F41, and compare it with that of other adenoviruses with respiratory (HAdV-C5) and ocular (HAdV-D26) tropisms. While the overall structures of hexon, penton base, and internal minor coat proteins IIIa and VIII are conserved, we observe partially ordered elements reinforcing the vertex region, which suggests their role in enhancing the physicochemical capsid stability of HAdV-F41. Unexpectedly, we find an organization of the external minor coat protein IX different from all previously characterized human and nonhuman mastadenoviruses. Knowledge of the structure of enteric adenoviruses provides a starting point for the design of vectors suitable for oral delivery or intestinal targeting. Cryo-EM structure of enteric adenovirus HAdV-F41 highlights structural variations among human adenoviruses.,Perez-Illana M, Martinez M, Condezo GN, Hernando-Perez M, Mangroo C, Brown M, Marabini R, San Martin C Sci Adv. 2021 Feb 24;7(9):eabd9421. doi: 10.1126/sciadv.abd9421. Print 2021 Feb. PMID:33627423[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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